Brucella melitensis UGPase inhibits the activation of NF-κB by modulating the ubiquitination of NEMO.

ABSTRACT:

Background

UTP-glucose-1-phosphoryl transferase (UGPase) catalyzes the synthesis of UDP-glucose, which is essential for generating the glycogen needed for the synthesis of bacterial lipopolysaccharide (LPS) and capsular polysaccharide, which play important roles in bacterial virulence. However, the molecular function of UGPase in Brucella is still unknown.

Results

In this study, the ubiquitination modification of host immune-related protein in cells infected with UGPase-deleted or wild-type Brucella was analyzed using ubiquitination proteomics technology. The ubiquitination modification level and type of NF-κB Essential Modulator (NEMO or Ikbkg), a molecule necessary for NF-κB signal activation, was evaluated using Coimmunoprecipitation, Western blot, and dual-Luciferase Ass

SUBMITTER: Zhou Y 

PROVIDER: S-EPMC8404259 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature